Linked Life Data

2842336

Source:http://linkedlifedata.com/resource/pubmed/id/2842336

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
1988-9-28
pubmed:abstractText
In cells transformed by either v-sis or c-sis, the majority of the newly synthesized platelet-derived growth factor (PDGF) receptors fail to reach the cell surface and are rapidly degraded. This rapid turnover (t1/2 less than 30 min) appears to result from interaction of the sis gene product with the PDGF receptor in the endoplasmic reticulum and/or Golgi apparatus during their intracellular routing from the endoplasmic reticulum to the plasma membrane or extracellular compartment. Several lines of evidence support this hypothesis. 1) Both the 160-kDa precursor and the intracellular 180-kDa mature form of the PDGF receptor possessed ligand binding activity for PDGF; 2) both the 160-kDa precursor and the 180-kDa mature form of the receptor in sis-transformed cells were found to be activated (phosphorylated); 3) protamine, a competitive inhibitor for PDGF or v-sis gene product binding to the cell-surface receptor, did not affect the rapid turnover of the PDGF receptor in sis-transformed cells; 4) suramin, an inhibitor for PDGF or v-sis gene product binding to the PDGF receptor, not only reversed the rapid turnover of the PDGF receptor in sis-transformed cells, but also increased the secretion of sis gene products; and 5) rapid turnover of the PDGF receptor was only observed in sis-transformed cells but not in cells transformed by other oncogenes. We suggest that the persistence of a mitogenic signal from cellular organelles, arising from the intracellular interaction of sis gene products with newly synthesized PDGF receptors, is the mechanism for autocrine transformation by sis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12608-18
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:2842336-Cell Line, Transformed, pubmed-meshheading:2842336-Cell Membrane, pubmed-meshheading:2842336-Cell Transformation, Neoplastic, pubmed-meshheading:2842336-Hexosaminidases, pubmed-meshheading:2842336-Humans, pubmed-meshheading:2842336-Immunosorbent Techniques, pubmed-meshheading:2842336-Molecular Weight, pubmed-meshheading:2842336-Oncogene Proteins v-sis, pubmed-meshheading:2842336-Phosphorylation, pubmed-meshheading:2842336-Platelet-Derived Growth Factor, pubmed-meshheading:2842336-Protein Precursors, pubmed-meshheading:2842336-Receptors, Cell Surface, pubmed-meshheading:2842336-Receptors, Platelet-Derived Growth Factor, pubmed-meshheading:2842336-Retroviridae, pubmed-meshheading:2842336-Retroviridae Proteins, pubmed-meshheading:2842336-Sarcoma Virus, Woolly Monkey, pubmed-meshheading:2842336-Suramin
pubmed:year
1988
pubmed:articleTitle
Rapid turnover of the platelet-derived growth factor receptor in sis-transformed cells and reversal by suramin. Implications for the mechanism of autocrine transformation.
pubmed:affiliation
E.A. Doisy Department of Biochemistry, St. Louis University School of Medicine, Missouri 63104.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't